node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
EPX82915.1 | EPX83141.1 | ruthe_03056 | ruthe_02758 | Cytochrome c, mono- and diheme variant. | Heme/copper-type cytochrome/quinol oxidase, subunit 2. | 0.951 |
EPX82915.1 | EPX84607.1 | ruthe_03056 | ruthe_01966 | Cytochrome c, mono- and diheme variant. | Ubiquinol-cytochrome c reductase, iron-sulfur subunit. | 0.992 |
EPX82915.1 | EPX84609.1 | ruthe_03056 | ruthe_01968 | Cytochrome c, mono- and diheme variant. | Cytochrome c1. | 0.900 |
EPX82915.1 | EPX84836.1 | ruthe_03056 | ruthe_01833 | Cytochrome c, mono- and diheme variant. | Hypothetical protein. | 0.947 |
EPX82915.1 | EPX84838.1 | ruthe_03056 | ruthe_01835 | Cytochrome c, mono- and diheme variant. | Sulfur dehydrogenase subunit SoxC. | 0.738 |
EPX82915.1 | EPX84839.1 | ruthe_03056 | ruthe_01836 | Cytochrome c, mono- and diheme variant. | Sulfur dehydrogenase subunit SoxD. | 0.994 |
EPX82915.1 | EPX87382.1 | ruthe_03056 | ruthe_00452 | Cytochrome c, mono- and diheme variant. | Cytochrome c oxidase, subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.951 |
EPX82915.1 | msrP | ruthe_03056 | ruthe_03335 | Cytochrome c, mono- and diheme variant. | Sulfite oxidase/related enzyme; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R [...] | 0.720 |
EPX83141.1 | EPX82915.1 | ruthe_02758 | ruthe_03056 | Heme/copper-type cytochrome/quinol oxidase, subunit 2. | Cytochrome c, mono- and diheme variant. | 0.951 |
EPX83141.1 | EPX84607.1 | ruthe_02758 | ruthe_01966 | Heme/copper-type cytochrome/quinol oxidase, subunit 2. | Ubiquinol-cytochrome c reductase, iron-sulfur subunit. | 0.973 |
EPX83141.1 | EPX84609.1 | ruthe_02758 | ruthe_01968 | Heme/copper-type cytochrome/quinol oxidase, subunit 2. | Cytochrome c1. | 0.974 |
EPX83141.1 | EPX84836.1 | ruthe_02758 | ruthe_01833 | Heme/copper-type cytochrome/quinol oxidase, subunit 2. | Hypothetical protein. | 0.679 |
EPX83141.1 | EPX84839.1 | ruthe_02758 | ruthe_01836 | Heme/copper-type cytochrome/quinol oxidase, subunit 2. | Sulfur dehydrogenase subunit SoxD. | 0.994 |
EPX83141.1 | EPX85765.1 | ruthe_02758 | ruthe_01694 | Heme/copper-type cytochrome/quinol oxidase, subunit 2. | Cytochrome c, mono- and diheme variant. | 0.984 |
EPX83141.1 | EPX86174.1 | ruthe_02758 | ruthe_00983 | Heme/copper-type cytochrome/quinol oxidase, subunit 2. | Cytochrome c, mono- and diheme variant. | 0.951 |
EPX83141.1 | EPX87382.1 | ruthe_02758 | ruthe_00452 | Heme/copper-type cytochrome/quinol oxidase, subunit 2. | Cytochrome c oxidase, subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.957 |
EPX84607.1 | EPX82915.1 | ruthe_01966 | ruthe_03056 | Ubiquinol-cytochrome c reductase, iron-sulfur subunit. | Cytochrome c, mono- and diheme variant. | 0.992 |
EPX84607.1 | EPX83141.1 | ruthe_01966 | ruthe_02758 | Ubiquinol-cytochrome c reductase, iron-sulfur subunit. | Heme/copper-type cytochrome/quinol oxidase, subunit 2. | 0.973 |
EPX84607.1 | EPX84609.1 | ruthe_01966 | ruthe_01968 | Ubiquinol-cytochrome c reductase, iron-sulfur subunit. | Cytochrome c1. | 0.999 |
EPX84607.1 | EPX84836.1 | ruthe_01966 | ruthe_01833 | Ubiquinol-cytochrome c reductase, iron-sulfur subunit. | Hypothetical protein. | 0.476 |